Important Molecules - Unit 1 Flashcards

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1
Q

Carbon Compounds

A
  • Forms covalent bond (two atoms sharing a pair of electrons)
  • Can form up to 4 bonds
  • Important in proteins, lipids, nucleic acids and carbs
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2
Q

4 Common Functional Groups

A
  • Hydroxyl (alcohol)
  • Amine (protein)
  • Carboxyl (protein)
  • Methyl (protein)
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3
Q

Metabolism

A
  • The sum of all reactions in an organism
  • Consists of ‘pathways’ where one molecule is turned into another
  • Two parts: Anabolism and Catabolism
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4
Q

Anabolism

A
  • Things coming together
  • Large molecule forms from small molecules with energy (ATP)
  • Condensation reactions
  • Ex. Photosynthesis
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5
Q

Catabolism

A
  • Things breaking apart
  • Large molecule turns into a small molecule and releases energy
  • Hydrolysis reactions
  • Ex. Digestion
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6
Q

Water

A
  • Polar (particle charges on each end, bent shape)
  • Covalent bonds
  • Attraction between h and o molecules are hydrogen bonds
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7
Q

Waters Unique Properties

A
  • Cohesive - Sticks to itself, ex. water transport in xylem
  • Adhesive - Sticks to other polar molecules, ex. adhesion to cellulose in plants
  • Thermal Properties
    1. High specific heat capacity - A large amount of energy is required to heat up, and release to cool
    2. High latent heat of vaporization - Large amounts of energy required to break h bonds and evaporate
  • Solvent properties - dissolves substances, dissolved polar covalent and ionic compounds, molecules form shells that prevent them from sticking together.
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8
Q

Hydrophilic vs. Hydrophobic

A

Hydrophilic - Substances that dissolve and adhere to water (salt)
Hydrophobic - Substances that can’t dissolve or adhere to water (lipids)

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9
Q

Transport of Substances in Blood Plasma

A

NaCl, AA, Glucose - Dissolved in plasma
O2 - Carried by hemoglobin
Fats, Cholesterol - Carried in Lipoprotein complexes in plasma

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10
Q

Carbohydrates

A
  • Made of C, H and O, often end in ‘ose’
  • Immediate energy source and energy storage
  • Builds other molecules
  • Used in cell membrane recognition and structures of plant cells
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11
Q

Types of Carbohydrates

A

Monosaccharides - 1 sugar unit, 3-7 C atoms, sweet taste, several polar -OH groups, soluble in water, ring structure
Disaccharides - 2 monosaccharides linked by condensation reactions, double ring structure
Polysaccharides - many monosaccharides

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12
Q

Examples of Polysaccharides

A

Cellulose - Unbranched, B D-glucose, chain alternating up and down, have ‘Cellulose Microfibils’ cellulose bonding parallel in hydrogen bonds
Starch - A D-glucose, same directions, two types:
1. Amylose - Plants store glucose in insoluble form, helix form
2. Amylopectin - Branched, glucose can be loaded or unloaded quickly due to many points
Glycogen - Branched, stores glucose in insoluble form in liver and muscle cells

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13
Q

Lipids

A
  • Non-polar, mostly hydrophobic hydrocarbons
  • Don’t form polymers
  • Types of lipids:
    Triglycerides, steroids, phospholipids
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14
Q

Triglycerides

A
  • Fats - Solid at room temp, liquid at body temp
  • Oils - Liquid at both temps
  • Used for nutrition, energy storage and insulation
  • Formed by 3 FAs and glycerol through a condensation reaction.
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15
Q

Fatty Acids

A
  • A long chain of C and H with a Carboxyl group, 4-24 C long
  • Saturated - Each C has an H, single bonded, straight chains, solid at room temp, animal sources
  • Unsaturated - Monounsaturated has 1 double bond, polyunsaturated has 2 or more double bonds, kinked chains, liquid at room temp, plant sources
    Cis-unsaturated FA - Naturally occurring , H on same side of the double bond, kinked chain
    Trans-unsaturated FA - Not naturally occurring, H on opposite side of double bond, straight chain, solid at room temp.
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16
Q

Proteins

A
  • Made up of AA’s containing an amino group, carboxyl group, carbon and R group
  • Polypeptides are chains of AA’s that form proteins linked by condensation reactions
  • Oligopeptide: 2-20 AA
  • Polypeptide: 20+ AA
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17
Q

Diversity of Amino Acids and Polypeptides

A
  • Unique R groups
  • 20 different AAs, 9 we have to consume
  • Some can be modified to make more AAs
  • Polypeptide is a chain of AAs linked by ribosomes, there are 20^n possible sequences, range from 20-10,000 AAs
  • Instructions are stored in base sequences
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18
Q

Shapes of Proteins

A
  • Shape determines function, 2 shapes:
    1. Globular (carrying), hydrophilic outside, hydrophobic inside, water-soluble, enzymes or carriers
    2. Fibrous (structure), elongated chain, water-insoluble, physically tough and stretchy
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19
Q

Proteomes

A
  • All proteins produced by organisms
  • Not fixed, varies over time
20
Q

Examples of Proteins and Functions

A

Rubisco - Catalyst, produces C
Insulin - Reduces glucose concentration
Immunoglobin - Produces antibodies
Rhodopsin - Pigment that absorbs light, nerve impulses
Collagen - Structure of skin and blood vessels
Spider Silk - Resistant to breakage

21
Q

Denaturation

A
  • Permanent change to protein
  • Heat, breaks bonds
  • pH, breaks bonds or causes new ones to form, changing the structure
22
Q

Active Sites and Enzymes

A
  • Globular proteins that catalyze reactions
  • 4000 different enzymes in a living cell
  • Substrates are the substances converted into products by the enzymes
  • Lock and Key: Enzyme and substrate are structurally the same and chemically attracted
  • Induced Fit: Less rigid, enzyme changes shape a bit
23
Q

Enzyme Activity

A
  1. Substrate binds to the active site by random collisions in the cytoplasm
  2. Substrate changes to products
  3. Products separate from the active site, the enzyme can bind again
24
Q

Factors Affecting Enzyme Activity

A
  1. Temp - Energy increases and so does probability to collide, too much heat can cause denaturation
  2. pH - Enzymes have a specific range, and will denaturate when out of it
  3. Substrate Concentration - More substrates will increase the rate of reactions, it will plateau once all are filled
  • Denaturation can result in a precipitate
25
Q

Immobilized Enzymes

A
  • Used in industry, attached to a material to limit movement or trapped in gels.
  • This is done to increase concentration, to recycle, to separate easier, and to stabilize
26
Q

Lactose-Free Milk

A
  • Lactose is mixed with lactase to create galactose and glucose
  • Increases sweetness, less crystallization in ice-cream, shortens production time for cheeses and yogurts
27
Q

DNA and RNA

A

DNA: Large molecules (2m/cell), genetic info, doesn’t leave the nucleus, ATGC
RNA: genetic info, mRNA, tRNA, rRNA, AUGC
Structure of a nucleotide: 5-C sugar, phosphate group, N-base, condensation reactions and phosphodiester bonds

28
Q

Difference Between DNA and RNA

A
  1. DNA has a deoxyribose sugar, and RNA has a ribose sugar
  2. DNA is double-stranded, RNA is single-stranded
  3. Have different bases
29
Q

Structure of DNA

A
  • Helix
  • Anti-parallel nucleotides linked by H bonding
30
Q

Replication of DNA

A
  • DNA splits and becomes 2 templates
  • Nucleotides added along templates
  • 2 strands form, each with half new, half old DNA (semi-conservative)
31
Q

Helicase

A
  • Separate the strands by breaking H bonds, requires energy, doughnut shape.
32
Q

DNA Polymerase

A
  • Multiple polypeptide subunits, joins nucleotides to template, moves in 5’ to 3’ direction, catalyzes phosphodiester bonds and proof reads, mistake only occur 1/1B.
33
Q

Transcription

A

-mRNA copies DNA, then moves to cytoplasm

34
Q

Translation

A
  1. mRNA binds to small subunit of ribosome
  2. tRNA and matching anticodon binds to ribosome
  3. Codon binds to ribosome (max 2)
  4. Ribosome transfers AA forming a peptide bond
  5. First tRNA is released
  6. New tRNA moves in
  7. Ribosome transfer AA chain to the next AA forming a peptide bond
  • 4,5 and 6 are repeated until STOP codon appears
35
Q

Ribosomes

A

2 subunits:
- Small, binds to mRNA
- Large, binds to tRNA and catalyzes peptide bonds

36
Q

Cell Respiration

A

Enzymes break Organic compounds into useable energy (ATP). ATP can’t be transferred; each must make their own.

37
Q

3 Types of Activity Energy (ATP) is Required For.

A
  1. Synthesizing large molecules
  2. Active transport across membranes
  3. Moving things through the cell
38
Q

ATP

A

Formed by linking a phosphate to an Adenosine and a diphosphate (ADP) with a high energy bond. Energy is easily released by splitting ATP. All processes release heat energy, raising body temp, but is soon lost in the environment; all cells require constant ATP.

39
Q

Anaerobic Respiration

A

Breaks down glucose without oxygen. Only 2 ATP is produced. Used in 3 circumstances:
1. Oxygen runs out in cells
2. Short, rapid burst of ATP needed
3. Oxygen-deficient environments
In animals, glucose is broken down into lactate.
In yeasts and plants, glucose turns into ethanol and CO2.
Lactate and ethanol are toxic and must be removed.

40
Q

Aerobic Respiration

A

Breaks down glucose using oxygen. Enzyme-controlled reactions, mostly in mitochondria. Up to 38 ATP produced. Glucose turns into CO2 and H2O(waste products, CO2 is excreted and H2O is used again).

41
Q

Respirometers

A

Used to calculate the rate of respiration by measuring the consumption of oxygen. Uses 6O2 and creates 6CO2, V doesn’t change, CO2 is absorbed and V decreases. Movement in capillary tubes / minute measures rate of O2 consumption.

42
Q

Photosynthesis and limiting factors

A

CO2 and water when met with sunlight energy turn into glucose and O2 (waste). Can be limited by temp, light intensity or CO2 concentration.

43
Q

Wavelengths of light

A

Violet is the shortest, red is the longest. Low frequency has longer wavelengths, less energy, and vice-versa. UV, X and gamma rays are harmful.

44
Q

Chlorophyll and photolysis

A

Chlorophyll absorbs all colours other than green. All oxygen in photosynthesis comes from photolysis, which releases electrons and oxygen.

45
Q

Impacts of photosynthesis

A
  • Creating a more stable atmosphere, 2% O to 21%.
  • More O2 formed the ozone layer
  • iron compounds in the oceans oxidized.